Travers AA - Search Results

1

Structural requirements for cooperative binding of HMG1 to DNA minicircles.

Webb M, Payet D, Lee KB, Travers AA, Thomas JO. Webb M, et al. Among authors: travers aa. J Mol Biol. 2001 May 25;309(1):79-88. doi: 10.1006/jmbi.2001.4667. J Mol Biol. 2001. PMID: 11491303

2

The recognition of distorted DNA structures by HMG-D: a footprinting and molecular modelling study.

Payet D, Hillisch A, Lowe N, Diekmann S, Travers A. Payet D, et al. J Mol Biol. 1999 Nov 19;294(1):79-91. doi: 10.1006/jmbi.1999.3246. J Mol Biol. 1999. PMID: 10556030

3

The acidic tail of the high mobility group protein HMG-D modulates the structural selectivity of DNA binding.

Payet D, Travers A. Payet D, et al. J Mol Biol. 1997 Feb 14;266(1):66-75. doi: 10.1006/jmbi.1996.0782. J Mol Biol. 1997. PMID: 9054971

4

HMG-D complexed to a bulge DNA: an NMR model.

Cerdan R, Payet D, Yang JC, Travers AA, Neuhaus D. Cerdan R, et al. Among authors: travers aa. Protein Sci. 2001 Mar;10(3):504-18. doi: 10.1110/ps.35501. Protein Sci. 2001. PMID: 11344319 Free PMC article.

5

HMG1 and 2, and related 'architectural' DNA-binding proteins.

Thomas JO, Travers AA. Thomas JO, et al. Among authors: travers aa. Trends Biochem Sci. 2001 Mar;26(3):167-74. doi: 10.1016/s0968-0004(01)01801-1. Trends Biochem Sci. 2001. PMID: 11246022 Review.

6

Structural insights into the mechanism of negative regulation of single-box high mobility group proteins by the acidic tail domain.

Stott K, Watson M, Bostock MJ, Mortensen SA, Travers A, Grasser KD, Thomas JO. Stott K, et al. J Biol Chem. 2014 Oct 24;289(43):29817-26. doi: 10.1074/jbc.M114.591115. Epub 2014 Sep 4. J Biol Chem. 2014. PMID: 25190813 Free PMC article.

7

DNA bending induced by high mobility group proteins studied by fluorescence resonance energy transfer.

Lorenz M, Hillisch A, Payet D, Buttinelli M, Travers A, Diekmann S. Lorenz M, et al. Biochemistry. 1999 Sep 14;38(37):12150-8. doi: 10.1021/bi990459+. Biochemistry. 1999. PMID: 10508419

8

PCR-based development of DNA substrates containing modified bases: an efficient system for investigating the role of the exocyclic groups in chemical and structural recognition by minor groove binding drugs and proteins.

Bailly C, Payet D, Travers AA, Waring MJ. Bailly C, et al. Among authors: travers aa. Proc Natl Acad Sci U S A. 1996 Nov 26;93(24):13623-8. doi: 10.1073/pnas.93.24.13623. Proc Natl Acad Sci U S A. 1996. PMID: 8942984 Free PMC article.

9

Highly disordered histone H1-DNA model complexes and their condensates.

Turner AL, Watson M, Wilkins OG, Cato L, Travers A, Thomas JO, Stott K. Turner AL, et al. Proc Natl Acad Sci U S A. 2018 Nov 20;115(47):11964-11969. doi: 10.1073/pnas.1805943115. Epub 2018 Oct 9. Proc Natl Acad Sci U S A. 2018. PMID: 30301810 Free PMC article.

10

The DNA-binding domain of human c-Abl tyrosine kinase promotes the interaction of a HMG chromosomal protein with DNA.

David-Cordonnier MH, Payet D, D'Halluin JC, Waring MJ, Travers AA, Bailly C. David-Cordonnier MH, et al. Among authors: travers aa. Nucleic Acids Res. 1999 Jun 1;27(11):2265-70. doi: 10.1093/nar/27.11.2265. Nucleic Acids Res. 1999. PMID: 10325413 Free PMC article.

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